View source for 6iqy


==High resolution structure of bilirubin oxidase from Myrothecium verrucaria - M467Q mutant, anaerobically prepared==
<StructureSection load='6iqy' size='340' side='right'caption='[[6iqy]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iqy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Albifimbria_verrucaria Albifimbria verrucaria]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5zd7 5zd7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IQY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iqy OCA], [https://pdbe.org/6iqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iqy RCSB], [https://www.ebi.ac.uk/pdbsum/6iqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iqy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLRO_ALBVE BLRO_ALBVE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bilirubin oxidase (BOD) belongs to the family of blue multicopper oxidases, and catalyzes the concomitant oxidation of bilirubin to biliverdin and the reduction of molecular oxygen to water via a four-electron reduction system. The active sites of BOD comprise four copper atoms; type I copper (T1Cu) forms a mononuclear site, and a cluster of three copper atoms forms a trinuclear center. In the present study, we determined the high-resolution crystal structures of BOD from the fungus Myrothecium verrucaria. We investigated wild-type (WT) BOD and a BOD mutant called Met467Gln, which is inactive against bilirubin. The structures revealed that a novel post-translational crosslink between Trp396 and His398 is formed in the vicinity of the T1Cu site in WT, whereas it is absent in the Met467Gln mutant. Our structural, computational, and electrochemical studies suggest that the His-Trp crosslink adjusts the redox potential of T1Cu to that of bilirubin to efficiently abstract electrons from the substrate.

Redox potential-dependent formation of an unusual His-Trp bond in bilirubin oxidase.,Akter M, Tokiwa T, Shoji M, Nishikawa K, Shigeta Y, Sakurai T, Higuchi Y, Kataoka K, Shibata N Chemistry. 2018 Aug 29. doi: 10.1002/chem.201803798. PMID:30156345<ref>PMID:30156345</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iqy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Albifimbria verrucaria]]
[[Category: Large Structures]]
[[Category: Akter M]]
[[Category: Higuchi Y]]
[[Category: Shibata N]]